4P5P
X-ray structure of Francisella tularensis Rapid Encystment Protein 24 KDa (REP24), gene product of FTN_0841
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.3.1 |
| Synchrotron site | ALS |
| Beamline | 8.3.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-04-05 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.1159 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 44.439, 44.439, 183.454 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 38.486 - 1.540 |
| R-factor | 0.1495 |
| Rwork | 0.147 |
| R-free | 0.19350 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1u9c |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.114 |
| Data reduction software | DENZO |
| Data scaling software | SCALA (3.2.5) |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.8.4_1496)) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 61.151 | 91.670 | 1.580 |
| High resolution limit [Å] | 1.500 | 4.740 | 1.500 |
| Rmerge | 0.095 | 0.056 | 0.226 |
| Total number of observations | 237816 | 10242 | 12964 |
| Number of reflections | 33819 | ||
| <I/σ(I)> | 13.4 | 26.2 | 1.9 |
| Completeness [%] | 96.9 | 99.8 | 82.9 |
| Redundancy | 7 | 8 | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 298 | 7.1% (w/v) PEG6000, 0.1M Na-Succinate pH 5.5, 0.58% Heptanoyl-N-methylglucamideMG7 |






